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Catalytically active MIP architectures

 
: Dechtrirat, Decha; Yarman, Aysu; Peng, Lei; Lettau, Kristian; Wollenberger, Ulla; Mosbach, Klaus; Scheller, Frieder W.

:

Turner, Anthony P.F. (Ed.):
Molecularly imprinted catalysts : Principles, syntheses, and applications
Amsterdam: Elsevier, 2016
ISBN: 978-0-12-801301-4
ISBN: 0-12-801444-X
ISBN: 978-0-12-801444-8
S.19-34
Englisch
Aufsatz in Buch
Fraunhofer IZI ()
biomimetic catalyst; enzyme; enzyme mimic; molecularly imprinted polymer

Abstract
Molecularly imprinted polymers (MIPs) have been developed mostly for the specific binding of the target, mimicking the function of antibodies. In addition to these “plastic antibodies,” completely synthetic catalysts have been created that mimic substrate conversion by enzymes. In this chapter, the following examples will be presented: (1) an esterolytic MIP for phenolic esters that is prepared using a transition state analogue as a template in an abzyme mimic; (2) MIPs using metal complexes and prosthetic groups, especially heme, in enzyme mimics; (3) a new MIP–enzyme architecture combining an enzyme containing an upper layer with a product-imprinted electropolymer on an amperometric electrode. The synergistic combination of the enzyme-catalyzed conversion of the drug aminopyrine with the MIP filter allows the interference-free measurement at a low electrode potential; and (4) protein-binding MIPs on top of a self-assembled monolayer (SAM) of an affinity ligand for the lectin concanavalin A (ConA) and the peroxidatic active hexameric tyrosine coordinated heme protein (HTHP). The oriented binding of the target protein to the SAM during formation of the MIP generates uniform binding sites. This is reflected by the high discrimination of similar lectins by the ConA-MIP and the realization of direct heterogeneous electron transfer and bioelectrocatalysis of peroxide reduction with the HTHP-MIP

: http://publica.fraunhofer.de/dokumente/N-399470.html